STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AOG28626.1acetyl-CoA hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (504 aa)    
Predicted Functional Partners:
AOG28204.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.970
sucC
succinate--CoA ligase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
   
 0.941
sucD
succinate--CoA ligase subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
   
 0.933
AOG27815.1
methylmalonyl-CoA mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.932
AOG29433.1
2-oxoglutarate ferredoxin oxidoreductase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.920
AOG29247.1
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.915
AOG28612.1
Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.915
AOG27567.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.913
AOG29114.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
   
 
 0.913
sdhA
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.910
Your Current Organism:
Cutibacterium avidum
NCBI taxonomy Id: 33010
Other names: ATCC 25577, Bacteroides avidus, C. avidum, CCUG 36754, CIP 103261, Corynebacterium avidum, DSM 4901, IFO 15671, Mycobacterium avidum, NBRC 15671, NCTC 11864, Propionibacterium avidum, Propionicibacterium avidum
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.